Control of EGF receptor signaling by clathrin-mediated endocytosis

Science

Volumn 274, Issue 5295, 1996, Pages 2086-2089

  Vieira, Amandio V ^a   Lamaze, Christophe ^a   Schmid, Sandra L ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; DIMERIZATION; ENDOCYTOSIS; INTERNALIZATION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR DOWN REGULATION; SIGNAL TRANSDUCTION;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ADAPTOR PROTEINS, VESICULAR TRANSPORT; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CELL DIVISION; CELL MEMBRANE; CLATHRIN; COATED PITS, CELL-MEMBRANE; DYNAMINS; ENDOCYTOSIS; ENZYME ACTIVATION; EPIDERMAL GROWTH FACTOR; GTP PHOSPHOHYDROLASES; HELA CELLS; HUMANS; ISOENZYMES; PHOSPHOLIPASE C; PHOSPHOLIPASE C GAMMA; PHOSPHORYLATION; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PHOSPHOTYROSINE; PROTEINS; RECEPTOR, EPIDERMAL GROWTH FACTOR; SIGNAL TRANSDUCTION;

ANIMALIA; MAMMALIA;

EID: 0030461226     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5295.2086     Document Type: Article

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33. 6 cells.
34. Cell extracts (1% Triton X-100) were immunoprecipitated [4 μg of immunoglobulin G (IgG) per 400 to 600 μg of lysate per 80 μl of immobilized Protein A/G or goat antibody to mouse IgG] and subjected to protein immunoblotting (1:2000 dilution of IgG) and ECL detection. Signals were quantitated with a Molecular Dynamics system.
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36. 3H]thymidine (1 μCi/ml) (Amersham) was added for the last 4 hours. Cells were then processed as described [A. Obermeier, I. Tinhofer, H. H. Grunicke, A. Ullrich, EMBO J. 15, 73 (1996)], and incorporated radioactivity was quantitated in the presence of ProteinPlus scintillant (Beckman).
37. 32P]MBP was then quantitated as described in Fig. 3.
38. We thank G. Gill and D. Cadena for the antibodies to human EGFR and T. Hunter for critical reading of the manuscript. Supported by National Cancer Institute grants CA58689 and CA69099 to S.L.S. A.V.V. was supported by the Human Frontier of Science Programme (grant LT 461/95), and C.L. was supported by the U.S. AMRMC (grant DAM17-94-J-4031). S.L.S. is an American Heart Association Established Investigator. This is The Scripps Research Institute manuscript number 10219-CB.